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PDBsum entry 1elb
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Hydrolase/hydrolase inhibitor
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PDB id
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1elb
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Contents |
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* Residue conservation analysis
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References listed in PDB file
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Key reference
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Title
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Analogous inhibitors of elastase do not always bind analogously.
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Authors
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C.Mattos,
B.Rasmussen,
X.Ding,
G.A.Petsko,
D.Ringe.
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Ref.
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Nat Struct Biol, 1994,
1,
55-58.
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PubMed id
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Note In the PDB file this reference is
annotated as "TO BE PUBLISHED".
The citation details given above were identified by an automated
search of PubMed on title and author
names, giving a
perfect match.
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Abstract
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It has been assumed that the structure of a single inhibitor complex is
sufficient to define the available subsites of an enzyme that has a unique
binding site and a uniquely defined mode for ligand binding--the specificity for
these subsites can thus be probed by kinetic experiments. Elastase is an enzyme
for which these traditional assumptions, which underlie such structural and
kinetic studies, do not hold. Three new crystal structures of elastase complexed
to chemically similar inhibitors with similar binding affinities reveal a
diversity of binding modes as well as two new subsites on elastase. The
existence of multiple binding sites and different binding modes for such similar
inhibitors indicates that researchers must proceed with caution when using
kinetics to map out protein subsites.
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Secondary reference #1
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Title
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Interaction of the peptide cf3-Leu-Ala-Nh-C6h4-Cf3 (tfla) with porcine pancreatic elastase. X-Ray studies at 1.8 a.
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Authors
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I.Li de la sierra,
E.Papamichael,
C.Sakarellos,
J.L.Dimicoli,
T.Prangé.
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Ref.
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J Mol Recognit, 1990,
3,
36-44.
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PubMed id
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Secondary reference #2
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Title
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Structure of native porcine pancreatic elastase at 1.65 a resolutions.
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Authors
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E.Meyer,
G.Cole,
R.Radhakrishnan,
O.Epp.
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Ref.
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Acta Crystallogr B, 1988,
44,
26-38.
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PubMed id
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Secondary reference #3
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Title
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Structure of the product complex of acetyl-Ala-Pro-Ala with porcine pancreatic elastase at 1.65 a resolution.
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Authors
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E.F.Meyer,
R.Radhakrishnan,
G.M.Cole,
L.G.Presta.
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Ref.
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J Mol Biol, 1986,
189,
533-539.
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PubMed id
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Secondary reference #4
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Title
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Crystallographic study of the binding of a trifluoroacetyl dipeptide anilide inhibitor with elastase.
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Authors
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D.L.Hughes,
L.C.Sieker,
J.Bieth,
J.L.Dimicoli.
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Ref.
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J Mol Biol, 1982,
162,
645-658.
[DOI no: ]
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PubMed id
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Figure 1.
FIG. 1. Superposition f the inhibitor molecule and some neighbouring residues on the final difference
map (p,- IF,/) or TFAP in the active site region. Contours ar drawn at estimated lrvrls of 0,;5, I.0 and
1.5 I?.
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Figure 3.
FIG. 3. Th active centre region in: (a) native elastase (pH 5.0); (b) tosyl-elastase; and (c) the
TFAl/elastase complex, TFAP.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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Secondary reference #5
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Title
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The indirect mechanism of action of the trifluoroacetyl peptides on elastase. Enzymatic and 19f nmr studies.
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Authors
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J.L.Dimicoli,
A.Renaud,
J.Bieth.
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Ref.
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Eur J Biochem, 1980,
107,
423-432.
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PubMed id
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Secondary reference #6
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Title
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The atomic structure of crystalline porcine pancreatic elastase at 2.5 a resolution: comparisons with the structure of alpha-Chymotrypsin.
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Authors
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L.Sawyer,
D.M.Shotton,
J.W.Campbell,
P.L.Wendell,
H.Muirhead,
H.C.Watson.
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Ref.
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J Mol Biol, 1978,
118,
137-208.
[DOI no: ]
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PubMed id
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Figure 1.
FIG. 1. The variation in he ean arent and heavy-atom structure amplitudes and in he
accurctcy of the hase etermination of the complete high resolution tosyl-elastse data set as a
unction of sin20/ha. (-A-A-), F,//2 -O-O--), lfHl --m--W--, --O--O---,
--A--/--) and E (-m-m--, -e-a--, -b-A-) are defined as in Tables 3 and 4.
The values or wa are iven by the right ordinate, nd those or 1Frl, lfnl and E, which are n he
same non-absolute scale, by the ordinate. A, CMBS-elastase; 0, ranyl tosyl-elastase;
H, uranyl CMBS-elastase.
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Figure 10.
IG. 10. Histograms of (a) x, b) yz, (c) x3.
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The above figures are
reproduced from the cited reference
with permission from Elsevier
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